node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AARI_05820 | AARI_28210 | AARI_05820 | AARI_28210 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | Malate dehydrogenase (oxaloacetate-decarboxylating); Catalyzes the oxidative decarboxylation of malate into pyruvate. Uses preferentially NAD and has the ability to decarboxylate oxaloacetate. | 0.836 |
AARI_05820 | gbh | AARI_05820 | AARI_05810 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | Guanidinobutyrase; Catalyses the following reaction: 4-guanidinobutanoate + H(2)O <=> 4-aminobutanoate + urea. The ortholog found in Arthrobacter sp. KUJ 8602 also acts on D-arginine, 3-guanidinopropionate and L-arginine; Belongs to the arginase family. | 0.889 |
AARI_05820 | ilvA | AARI_05820 | AARI_07480 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | Catalyzes the conversion of threonine into 2-oxobutanoate. Involved in isoleucine biosynthesis. The enzyme from a number of sources also acts on L-serine. | 0.941 |
AARI_05820 | ilvC | AARI_05820 | AARI_13810 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.977 |
AARI_05820 | ilvN | AARI_05820 | AARI_13800 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | Acetolactate synthase catalyses the first common step in the biosynthesis of the 3 branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. The resulting products are 2-acetolactate and 2-aceto2-hydroxybutanoate. | 0.943 |
AARI_05820 | leuA | AARI_05820 | AARI_16790 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.902 |
AARI_05820 | leuB | AARI_05820 | AARI_14240 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | 3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. | 0.953 |
AARI_05820 | lldD | AARI_05820 | AARI_31060 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | L-lactate dehydrogenase (cytochrome); Catalyses the conversion of L-lactate to pyruvate. Probable quinone-dependent lactate dehydrogenase, functionning when lactate is used as a carbon and energy source. | 0.873 |
AARI_05820 | poxB | AARI_05820 | AARI_17870 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | Pyruvate dehydrogenase (cytochrome); TPP-binding module. Catalyzes the formation of acetate from pyruvate (catalytic activity: pyruvate + ferricytochrome b1 + H2O = acetate + CO2 + ferrocytochrome b1). | 0.855 |
AARI_05820 | pyk | AARI_05820 | AARI_19410 | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | Pyruvate kinase; Catalyses the conversion of phosphoenolpyruvate to pyruvate with the concomitant phosphorylation of ADP to ATP. | 0.837 |
AARI_28210 | AARI_05820 | AARI_28210 | AARI_05820 | Malate dehydrogenase (oxaloacetate-decarboxylating); Catalyzes the oxidative decarboxylation of malate into pyruvate. Uses preferentially NAD and has the ability to decarboxylate oxaloacetate. | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | 0.836 |
AARI_28210 | ilvN | AARI_28210 | AARI_13800 | Malate dehydrogenase (oxaloacetate-decarboxylating); Catalyzes the oxidative decarboxylation of malate into pyruvate. Uses preferentially NAD and has the ability to decarboxylate oxaloacetate. | Acetolactate synthase catalyses the first common step in the biosynthesis of the 3 branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. The resulting products are 2-acetolactate and 2-aceto2-hydroxybutanoate. | 0.822 |
AARI_28210 | leuA | AARI_28210 | AARI_16790 | Malate dehydrogenase (oxaloacetate-decarboxylating); Catalyzes the oxidative decarboxylation of malate into pyruvate. Uses preferentially NAD and has the ability to decarboxylate oxaloacetate. | 2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. | 0.826 |
AARI_28210 | lldD | AARI_28210 | AARI_31060 | Malate dehydrogenase (oxaloacetate-decarboxylating); Catalyzes the oxidative decarboxylation of malate into pyruvate. Uses preferentially NAD and has the ability to decarboxylate oxaloacetate. | L-lactate dehydrogenase (cytochrome); Catalyses the conversion of L-lactate to pyruvate. Probable quinone-dependent lactate dehydrogenase, functionning when lactate is used as a carbon and energy source. | 0.910 |
AARI_28210 | poxB | AARI_28210 | AARI_17870 | Malate dehydrogenase (oxaloacetate-decarboxylating); Catalyzes the oxidative decarboxylation of malate into pyruvate. Uses preferentially NAD and has the ability to decarboxylate oxaloacetate. | Pyruvate dehydrogenase (cytochrome); TPP-binding module. Catalyzes the formation of acetate from pyruvate (catalytic activity: pyruvate + ferricytochrome b1 + H2O = acetate + CO2 + ferrocytochrome b1). | 0.918 |
AARI_28210 | pyk | AARI_28210 | AARI_19410 | Malate dehydrogenase (oxaloacetate-decarboxylating); Catalyzes the oxidative decarboxylation of malate into pyruvate. Uses preferentially NAD and has the ability to decarboxylate oxaloacetate. | Pyruvate kinase; Catalyses the conversion of phosphoenolpyruvate to pyruvate with the concomitant phosphorylation of ADP to ATP. | 0.949 |
gbh | AARI_05820 | AARI_05810 | AARI_05820 | Guanidinobutyrase; Catalyses the following reaction: 4-guanidinobutanoate + H(2)O <=> 4-aminobutanoate + urea. The ortholog found in Arthrobacter sp. KUJ 8602 also acts on D-arginine, 3-guanidinopropionate and L-arginine; Belongs to the arginase family. | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | 0.889 |
ilvA | AARI_05820 | AARI_07480 | AARI_05820 | Catalyzes the conversion of threonine into 2-oxobutanoate. Involved in isoleucine biosynthesis. The enzyme from a number of sources also acts on L-serine. | Thiamine pyrophosphate binding domain-containing protein; Domain present in thiamine pyrophosphate-requiring enzymes (acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase); Belongs to the TPP enzyme family. | 0.941 |
ilvA | ilvC | AARI_07480 | AARI_13810 | Catalyzes the conversion of threonine into 2-oxobutanoate. Involved in isoleucine biosynthesis. The enzyme from a number of sources also acts on L-serine. | Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | 0.840 |
ilvA | ilvN | AARI_07480 | AARI_13800 | Catalyzes the conversion of threonine into 2-oxobutanoate. Involved in isoleucine biosynthesis. The enzyme from a number of sources also acts on L-serine. | Acetolactate synthase catalyses the first common step in the biosynthesis of the 3 branched-chain amino acids. The first step involves the condensation of either pyruvate or 2-ketobutyrate with the two-carbon hydroxyethyl fragment derived from another pyruvate molecule, covalently bound to the coenzyme thiamine diphosphate. The resulting products are 2-acetolactate and 2-aceto2-hydroxybutanoate. | 0.977 |